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| Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane |
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| Author(s): Czajkowsky DM, Hotze EM, Shao ZF, Tweten RK |
| Source: EMBO JOURNAL Volume: 23 Issue: 16 Pages: 3206-3215 Published: AUG 18 2004 |
| Times Cited: 48 References: 41 |
| Abstract: Perfringolysin O (PFO) is a prototype of the large family of pore-forming cholesterol-dependent cytolysins (CDCs). A central enigma of the cytolytic mechanism of the CDCs is that their membrane-spanning beta-hairpins (the transmembrane amphipathic beta-hairpins (TMHs)) appear to be similar to40 Angstrom too far above the membrane surface to cross the bilayer and form the pore. We now present evidence, using atomic force microscopy (AFM), of a significant difference in the height by which the prepore and pore protrude from the membrane surface: 113+/-5 Angstrom for the prepore but only 73+/-5 Angstrom for the pore. Time-lapse AFM micrographs show this change in height in real time. Moreover, the monomers in both complexes exhibit nearly identical surface features and these results in combination with those of spectrofluorimetric analyses indicate that the monomers remain in a perpendicular orientation to the bilayer plane during this transition. Therefore, the PFO undergoes a vertical collapse that brings its TMHs to the membrane surface so that they can extend across the bilayer to form the beta-barrel pore. |
| Document Type: Article |
| Language: English |
| Reprint Address: Shao, ZF (reprint author), Univ Virginia, Sch Med, Dept Mol Physiol & Biol Phys, Room 480,Jordan Hall, Charlottesville, VA 22908 USA |
Addresses:
1. Univ Virginia, Sch Med, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22908 USA
2. Univ Oklahoma, Hlth Sci Ctr, Dept Microbiol & Immunol, Oklahoma City, OK 73104 USA |
| Publisher: NATURE PUBLISHING GROUP, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 USA |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: 852CK |
| ISSN: 0261-4189 |
| DOI: 10.1038/sj.emboj.7600350 |
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